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2vc3

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Revision as of 10:01, 5 August 2016

RICIN A-CHAIN (RECOMBINANT) E177D MUTANT WITH A BOUND ACETATE

Structural highlights

2vc3 is a 1 chain structure with sequence from Castor bean. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	1apg, 1br5, 1br6, 1j1m, 1obs, 1obt, 1uq4, 1zam, 1zb2, 2aai, 1fmp, 1ifs, 1ift, 1ifu, 1il3, 1il4, 1il5, 1il9, 1rtc, 1uq5, 1zb0, 2vc4
Activity:	rRNA N-glycosylase, with EC number 3.2.2.22
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[RICI_RICCO] Ricin is highly toxic to animal cells and to a lesser extent to plant cells. The A chain acts as a glycosidase that removes a specific adenine residue from an exposed loop of the 28S rRNA (A4324 in mammals), leading to rRNA breakage. As this loop is involved in elongation factor binding, modified ribosomes are catalytically inactive and unable to support protein synthesis. The A chain can inactivate a few thousand ribosomes per minute, faster than the cell can make new ones. Therefore a single A chain molecule can kill an animal cell. The B chain binds to beta-D-galactopyranoside moieties on cell surface glycoproteins and glycolipids and facilitates the entry into the cell of the A chain; B chains are also responsible for cell agglutination (Lectin activity).

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Ricin is a heterodimeric plant protein that is potently toxic to mammalian cells. Toxicity results from the catalytic depurination of eukaryotic ribosomes by ricin toxin A chain (RTA) that follows toxin endocytosis to, and translocation across, the endoplasmic reticulum membrane. To ultimately identify proteins required for these later steps in the entry process, it will be useful to express the catalytic subunit within the endoplasmic reticulum of yeast cells in a manner that initially permits cell growth. A subsequent switch in conditions to provoke innate toxin action would permit only those strains containing defects in genes normally essential for toxin retro-translocation, refolding or degradation to survive. As a route to such a screen, several RTA mutants with reduced catalytic activity have previously been isolated. Here we report the use of Saccharomyces cerevisiae to isolate temperature-dependent mutants of endoplasmic reticulum-targeted RTA. Two such toxin mutants with opposing phenotypes were isolated. One mutant RTA (RTAF108L/L151P) allowed the yeast cells that express it to grow at 37 degrees C, whereas the same cells did not grow at 23 degrees C. Both mutations were required for temperature-dependent growth. The second toxin mutant (RTAE177D) allowed cells to grow at 23 degrees C but not at 37 degrees C. Interestingly, RTAE177D has been previously reported to have reduced catalytic activity, but this is the first demonstration of a temperature-sensitive phenotype. To provide a more detailed characterization of these mutants we have investigated their N-glycosylation, stability, catalytic activity and, where appropriate, a three-dimensional structure. The potential utility of these mutants is discussed.

The isolation and characterization of temperature-dependent ricin A chain molecules in Saccharomyces cerevisiae.,Allen SC, Moore KA, Marsden CJ, Fulop V, Moffat KG, Lord JM, Ladds G, Roberts LM FEBS J. 2007 Nov;274(21):5586-99. Epub 2007 Oct 4. PMID:17916187^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Allen SC, Moore KA, Marsden CJ, Fulop V, Moffat KG, Lord JM, Ladds G, Roberts LM. The isolation and characterization of temperature-dependent ricin A chain molecules in Saccharomyces cerevisiae. FEBS J. 2007 Nov;274(21):5586-99. Epub 2007 Oct 4. PMID:17916187 doi:10.1111/j.1742-4658.2007.06080.x

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2vc3"

@@ Line 1: / Line 1: @@
 ==RICIN A-CHAIN (RECOMBINANT) E177D MUTANT WITH A BOUND ACETATE==
 <StructureSection load='2vc3' size='340' side='right' caption='[[2vc3]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2vc3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ricinus_communis Ricinus communis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VC3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VC3 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2vc3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Castor_bean Castor bean]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VC3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VC3 FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1apg|1apg]], [[1br5|1br5]], [[1br6|1br6]], [[1j1m|1j1m]], [[1obs|1obs]], [[1obt|1obt]], [[1uq4|1uq4]], [[1zam|1zam]], [[1zb2|1zb2]], [[2aai|2aai]], [[1fmp|1fmp]], [[1ifs|1ifs]], [[1ift|1ift]], [[1ifu|1ifu]], [[1il3|1il3]], [[1il4|1il4]], [[1il5|1il5]], [[1il9|1il9]], [[1rtc|1rtc]], [[1uq5|1uq5]], [[1zb0|1zb0]], [[2vc4|2vc4]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/rRNA_N-glycosylase rRNA N-glycosylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.2.22 3.2.2.22] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2vc3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vc3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2vc3 RCSB], [http://www.ebi.ac.uk/pdbsum/2vc3 PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2vc3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vc3 OCA], [http://pdbe.org/2vc3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vc3 RCSB], [http://www.ebi.ac.uk/pdbsum/2vc3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2vc3 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 18: / Line 19: @@
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
-</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2vc3 ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 28: / Line 29: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2vc3" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 35: / Line 37: @@
 __TOC__
 </StructureSection>
-[[Category: Ricinus communis]]
+[[Category: Castor bean]]
 [[Category: RRNA N-glycosylase]]
 [[Category: Fulop, V]]

2vc3

From Proteopedia

Revision as of 10:01, 5 August 2016

RICIN A-CHAIN (RECOMBINANT) E177D MUTANT WITH A BOUND ACETATE

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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